KLK1_HUMAN
ID KLK1_HUMAN Reviewed; 262 AA.
AC P06870; Q66US9; Q86U61; Q8TCV8; Q9BS53; Q9NQU4; Q9UD19; Q9UMJ1;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Kallikrein-1;
DE EC=3.4.21.35;
DE AltName: Full=Kidney/pancreas/salivary gland kallikrein;
DE AltName: Full=Tissue kallikrein;
DE Flags: Precursor;
GN Name=KLK1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-145 AND GLU-186.
RC TISSUE=Pancreas;
RX PubMed=3004571; DOI=10.1021/bi00348a030;
RA Fukushima D., Kitamura N., Nakanishi S.;
RT "Nucleotide sequence of cloned cDNA for human pancreatic kallikrein.";
RL Biochemistry 24:8037-8043(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-145.
RC TISSUE=Kidney;
RX PubMed=2898948; DOI=10.1021/bi00409a003;
RA Evans B.A., Yun Z.X., Close J.A., Tregear G.W., Kitamura N., Nakanishi S.,
RA Callen D.F., Baker E., Hyland V.J., Sutherland G.R., Richards R.I.;
RT "Structure and chromosomal localization of the human renal kallikrein
RT gene.";
RL Biochemistry 27:3124-3129(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Salivary gland;
RX PubMed=2686621; DOI=10.1042/bj2620787;
RA Angermann A., Bergmann C., Appelhans H.;
RT "Cloning and expression of human salivary-gland kallikrein in Escherichia
RT coli.";
RL Biochem. J. 262:787-793(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=7749372;
RA Chen L.-M., Murray S.R., Chai K.X., Chao L., Chao J.;
RT "Molecular cloning and characterization of a novel kallikrein transcript in
RT colon and its distribution in human tissues.";
RL Braz. J. Med. Biol. Res. 27:1829-1838(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11006094; DOI=10.1006/bbrc.2000.3448;
RA Yousef G.M., Chang A., Scorilas A., Diamandis E.P.;
RT "Genomic organization of the human kallikrein gene family on chromosome
RT 19q13.3-q13.4.";
RL Biochem. Biophys. Res. Commun. 276:125-133(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054574; DOI=10.1016/s0378-1119(00)00382-6;
RA Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J., Moss P.,
RA Paeper B., Wang K.;
RT "Sequencing and expression analysis of the serine protease gene cluster
RT located in chromosome 19q13 region.";
RL Gene 257:119-130(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-145 AND GLU-186.
RA Li T., Du G., Dai Y.;
RT "Kallikrein cDNA from the pancreas of a Chinese patient.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-145.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-145.
RG SeattleSNPs variation discovery resource;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-145.
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-262 (ISOFORM 1), AND VARIANTS GLN-145 AND
RP GLU-186.
RC TISSUE=Kidney;
RX PubMed=3853975; DOI=10.1089/dna.1985.4.445;
RA Baker A.R., Shine J.;
RT "Human kidney kallikrein: cDNA cloning and sequence analysis.";
RL DNA 4:445-450(1985).
RN [13]
RP PROTEIN SEQUENCE OF 25-262 (ISOFORM 1), AND GLYCOSYLATION AT SER-93;
RP ASN-102; SER-104; ASN-108; ASN-165 AND SER-167.
RC TISSUE=Urine;
RX PubMed=3163150;
RA Kellermann J., Lottspeich F., Geiger R., Deutzmann R.;
RT "Human urinary kallikrein -- amino acid sequence and carbohydrate
RT attachment sites.";
RL Protein Seq. Data Anal. 1:177-182(1988).
RN [14]
RP PROTEIN SEQUENCE OF 25-262 (ISOFORM 1).
RC TISSUE=Urine;
RX PubMed=2666327; DOI=10.1111/j.1399-3011.1989.tb01277.x;
RA Lu H.S., Lin F.-K., Chao L., Chao J.;
RT "Human urinary kallikrein. Complete amino acid sequence and sites of
RT glycosylation.";
RL Int. J. Pept. Protein Res. 33:237-249(1989).
RN [15]
RP PROTEIN SEQUENCE OF 25-55 (ISOFORM 1).
RC TISSUE=Urine;
RX PubMed=393608;
RA Lottspeich F., Geiger R., Henschen A., Kutzbach C.;
RT "N-terminal amino acid sequence of human urinary kallikrein homology with
RT other serine proteases.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1947-1950(1979).
RN [16]
RP PROTEIN SEQUENCE OF 28-47 (ISOFORM 1).
RC TISSUE=Urine;
RX PubMed=3635530; DOI=10.1093/oxfordjournals.jbchem.a135563;
RA Takahashi S., Irie A., Katayama Y., Ito K., Miyake Y.;
RT "N-terminal amino acid sequence of human urinary prokallikrein.";
RL J. Biochem. 99:989-992(1986).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-262, GLYCOSYLATION AT ASN-108,
RP AND DISULFIDE BONDS.
RX PubMed=15651049; DOI=10.1002/prot.20368;
RA Laxmikanthan G., Blaber S.I., Bernett M.J., Scarisbrick I.A., Juliano M.A.,
RA Blaber M.;
RT "1.70 A X-ray structure of human apo kallikrein 1: structural changes upon
RT peptide inhibitor/substrate binding.";
RL Proteins 58:802-814(2005).
RN [18]
RP CHARACTERIZATION OF VARIANTS HIS-77 AND GLN-145, AND POLYMORPHISM.
RX PubMed=11912256; DOI=10.1681/asn.v134968;
RA Slim R., Torremocha F., Moreau T., Pizard A., Hunt S.C., Vuagnat A.,
RA Williams G.H., Gauthier F., Jeunemaitre X., Alhenc-Gelas F.;
RT "Loss-of-function polymorphism of the human kallikrein gene with reduced
RT urinary kallikrein activity.";
RL J. Am. Soc. Nephrol. 13:968-976(2002).
RN [19]
RP POLYMORPHISM.
RX PubMed=15765151; DOI=10.1172/jci200523669;
RA Azizi M., Boutouyrie P., Bissery A., Agharazii M., Verbeke F., Stern N.,
RA Bura-Riviere A., Laurent S., Alhenc-Gelas F., Jeunemaitre X.;
RT "Arterial and renal consequences of partial genetic deficiency in tissue
RT kallikrein activity in humans.";
RL J. Clin. Invest. 115:780-787(2005).
CC -!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in
CC kininogen to release Lys-bradykinin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule
CC substrates. Highly selective action to release kallidin (lysyl-
CC bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-
CC Xaa.; EC=3.4.21.35;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P06870-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06870-2; Sequence=VSP_037483;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in pancreas, salivary
CC glands, kidney, colon, prostate gland, testis, spleen and the colon
CC adenocarcinoma cell line T84. {ECO:0000269|PubMed:7749372}.
CC -!- PTM: The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are
CC probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was
CC detected with the corresponding peptides but not located.
CC {ECO:0000269|PubMed:15651049, ECO:0000269|PubMed:3163150}.
CC -!- POLYMORPHISM: Genetic variations in KLK1 are the cause of a decreased
CC in urinary kallikrein activity [MIM:615953]. The His-77 mutation
CC dramatically reduces the activity of the enzyme in the urine. There is
CC a 50 to 60% reduction in urinary kallikrein activity in His-77
CC individuals, but renal and hormonal adaptation to dietary changes in
CC sodium and potassium are unaffected. However, in studies of brachial
CC artery function, His-77 individuals consistently exhibited an increase
CC in wall shear stress and a paradoxical reduction in artery diameter and
CC lumen compared to Arg-77 individuals. This partial genetic deficiency
CC in kallikrein activity is associated with a form of arterial
CC dysfunction involving inappropriate inward remodeling of the brachial
CC artery despite a chronic increase in shear stress.
CC {ECO:0000269|PubMed:11912256, ECO:0000269|PubMed:15765151}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Kallikrein entry;
CC URL="https://en.wikipedia.org/wiki/Kallikrein";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/klk1/";
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DR EMBL; M25629; AAA36136.1; -; mRNA.
DR EMBL; M33109; AAA59455.1; -; Genomic_DNA.
DR EMBL; M33105; AAA59455.1; JOINED; Genomic_DNA.
DR EMBL; M33106; AAA59455.1; JOINED; Genomic_DNA.
DR EMBL; M33107; AAA59455.1; JOINED; Genomic_DNA.
DR EMBL; M33108; AAA59455.1; JOINED; Genomic_DNA.
DR EMBL; X13561; CAA31912.1; -; mRNA.
DR EMBL; AF277050; AAF86333.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33353.1; -; Genomic_DNA.
DR EMBL; AY703451; AAU12569.1; -; mRNA.
DR EMBL; BT007253; AAP35917.1; -; mRNA.
DR EMBL; AY094609; AAM11874.1; -; Genomic_DNA.
DR EMBL; AC010325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005313; AAH05313.1; -; mRNA.
DR EMBL; M12706; AAA59201.1; -; mRNA.
DR CCDS; CCDS12804.1; -. [P06870-1]
DR PIR; A24696; KQHU.
DR PIR; B24696; B24696.
DR RefSeq; NP_002248.1; NM_002257.3. [P06870-1]
DR PDB; 1SPJ; X-ray; 1.70 A; A=25-262.
DR PDBsum; 1SPJ; -.
DR AlphaFoldDB; P06870; -.
DR SMR; P06870; -.
DR BioGRID; 110016; 48.
DR STRING; 9606.ENSP00000301420; -.
DR BindingDB; P06870; -.
DR ChEMBL; CHEMBL2319; -.
DR DrugBank; DB01370; Aluminium.
DR DrugBank; DB14517; Aluminium phosphate.
DR DrugBank; DB14518; Aluminum acetate.
DR DrugBank; DB06728; Aniline.
DR DrugBank; DB06692; Aprotinin.
DR DrugBank; DB03127; Benzamidine.
DR DrugBank; DB06245; Lanoteplase.
DR DrugBank; DB12598; Nafamostat.
DR DrugCentral; P06870; -.
DR GuidetoPHARMACOLOGY; 2865; -.
DR MEROPS; S01.160; -.
DR GlyConnect; 172; 15 N-Linked glycans.
DR GlyGen; P06870; 7 sites, 28 N-linked glycans (4 sites).
DR iPTMnet; P06870; -.
DR PhosphoSitePlus; P06870; -.
DR BioMuta; KLK1; -.
DR DMDM; 269849612; -.
DR jPOST; P06870; -.
DR MassIVE; P06870; -.
DR PaxDb; P06870; -.
DR PeptideAtlas; P06870; -.
DR PRIDE; P06870; -.
DR ProteomicsDB; 51938; -. [P06870-1]
DR ProteomicsDB; 51939; -. [P06870-2]
DR Antibodypedia; 32372; 428 antibodies from 37 providers.
DR DNASU; 3816; -.
DR Ensembl; ENST00000301420.3; ENSP00000301420.1; ENSG00000167748.11. [P06870-1]
DR GeneID; 3816; -.
DR KEGG; hsa:3816; -.
DR MANE-Select; ENST00000301420.3; ENSP00000301420.1; NM_002257.4; NP_002248.1.
DR UCSC; uc002ptk.3; human. [P06870-1]
DR CTD; 3816; -.
DR DisGeNET; 3816; -.
DR GeneCards; KLK1; -.
DR HGNC; HGNC:6357; KLK1.
DR HPA; ENSG00000167748; Group enriched (pancreas, salivary gland).
DR MalaCards; KLK1; -.
DR MIM; 147910; gene.
DR MIM; 615953; phenotype.
DR neXtProt; NX_P06870; -.
DR OpenTargets; ENSG00000167748; -.
DR PharmGKB; PA224; -.
DR VEuPathDB; HostDB:ENSG00000167748; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; P06870; -.
DR OMA; WQVALYH; -.
DR OrthoDB; 1129026at2759; -.
DR PhylomeDB; P06870; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.35; 2681.
DR PathwayCommons; P06870; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR SignaLink; P06870; -.
DR BioGRID-ORCS; 3816; 6 hits in 1079 CRISPR screens.
DR ChiTaRS; KLK1; human.
DR EvolutionaryTrace; P06870; -.
DR GeneWiki; KLK1; -.
DR GenomeRNAi; 3816; -.
DR Pharos; P06870; Tchem.
DR PRO; PR:P06870; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P06870; protein.
DR Bgee; ENSG00000167748; Expressed in body of pancreas and 133 other tissues.
DR ExpressionAtlas; P06870; baseline and differential.
DR Genevisible; P06870; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT PROPEP 19..24
FT /note="Activation peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000027923"
FT CHAIN 25..262
FT /note="Kallikrein-1"
FT /id="PRO_0000027924"
FT DOMAIN 25..259
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 65
FT /note="Charge relay system"
FT ACT_SITE 120
FT /note="Charge relay system"
FT ACT_SITE 214
FT /note="Charge relay system"
FT CARBOHYD 93
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3163150"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3163150"
FT CARBOHYD 104
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3163150"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15651049,
FT ECO:0000269|PubMed:3163150"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:3163150"
FT CARBOHYD 167
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:3163150"
FT DISULFID 31..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15651049"
FT DISULFID 50..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15651049"
FT DISULFID 153..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15651049"
FT DISULFID 185..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15651049"
FT DISULFID 210..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274,
FT ECO:0000269|PubMed:15651049"
FT VAR_SEQ 1..69
FT /note="MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGG
FT ILVHRQWVLTAAHCISD -> MLPCPIPFSPSRLLIPPFPSFPS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:7749372"
FT /id="VSP_037483"
FT VARIANT 77
FT /note="R -> H (associated with a significant decrease in
FT urinary kallikrein activity; dbSNP:rs5515)"
FT /evidence="ECO:0000269|PubMed:11912256"
FT /id="VAR_014567"
FT VARIANT 145
FT /note="E -> Q (not associated with changes in urinary
FT kallikrein activity; dbSNP:rs5516)"
FT /evidence="ECO:0000269|PubMed:11912256,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2898948,
FT ECO:0000269|PubMed:3004571, ECO:0000269|PubMed:3853975,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0000269|Ref.9"
FT /id="VAR_006625"
FT VARIANT 186
FT /note="K -> E (in dbSNP:rs5517)"
FT /evidence="ECO:0000269|PubMed:3004571,
FT ECO:0000269|PubMed:3853975, ECO:0000269|Ref.7"
FT /id="VAR_006626"
FT VARIANT 193
FT /note="V -> E (in dbSNP:rs5518)"
FT /id="VAR_014568"
FT CONFLICT 114
FT /note="D -> N (in Ref. 7; AAU12569)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="V -> F (in Ref. 7; AAU12569)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> V (in Ref. 8; AAP35917 and 11; AAH05313)"
FT /evidence="ECO:0000305"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1SPJ"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1SPJ"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1SPJ"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:1SPJ"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1SPJ"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1SPJ"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:1SPJ"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:1SPJ"
SQ SEQUENCE 262 AA; 28890 MW; 7D8A715E9E104D60 CRC64;
MWFLVLCLAL SLGGTGAAPP IQSRIVGGWE CEQHSQPWQA ALYHFSTFQC GGILVHRQWV
LTAAHCISDN YQLWLGRHNL FDDENTAQFV HVSESFPHPG FNMSLLENHT RQADEDYSHD
LMLLRLTEPA DTITDAVKVV ELPTEEPEVG STCLASGWGS IEPENFSFPD DLQCVDLKIL
PNDECKKAHV QKVTDFMLCV GHLEGGKDTC VGDSGGPLMC DGVLQGVTSW GYVPCGTPNK
PSVAVRVLSY VKWIEDTIAE NS
